STYL2_DANRE
ID STYL2_DANRE Reviewed; 1100 AA.
AC F1QWM2;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Serine/threonine/tyrosine-interacting-like protein 2;
DE AltName: Full=Inactive dual specificity phosphatase 27 {ECO:0000305};
GN Name=styxl2; Synonyms=dusp27 {ECO:0000312|ZFIN:ZDB-GENE-140513-1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=24203884; DOI=10.1242/dmm.013235;
RA Fero K., Bergeron S.A., Horstick E.J., Codore H., Li G.H., Ono F.,
RA Dowling J.J., Burgess H.A.;
RT "Impaired embryonic motility in dusp27 mutants reveals a developmental
RT defect in myofibril structure.";
RL Dis. Model. Mech. 7:289-298(2014).
CC -!- FUNCTION: Required for myofiber maturation.
CC {ECO:0000269|PubMed:24203884}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000305|PubMed:24203884}.
CC -!- TISSUE SPECIFICITY: Expressed in muscle fibers in a regular striated
CC pattern (at protein level). {ECO:0000269|PubMed:24203884}.
CC -!- DEVELOPMENTAL STAGE: At 24 hpf, expressed in the somites and several
CC regions of the brain, including the midbrain roof (tectum).
CC {ECO:0000269|PubMed:24203884}.
CC -!- DISRUPTION PHENOTYPE: At 2 dpf, morphants are morphologically normal
CC but show pericardial edema and tail curvature. They exhibit near
CC complete paralysis at embryonic and larval stages, producing extremely
CC low levels of spontaneous coiling movements and a greatly diminished
CC touch response. They show a severe disorganization of the contractile
CC apparatus in muscle fibers. Sarcomeric structures in mutants are almost
CC entirely absent and only rare triads are observed.
CC {ECO:0000269|PubMed:24203884}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
CC -!- CAUTION: Ser-234 is present instead of the conserved Cys which is
CC expected to be an active site residue suggesting that this protein has
CC lost its phosphatase activity. {ECO:0000305}.
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DR EMBL; CABZ01080368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABZ01080369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003197655.1; XM_003197607.4.
DR AlphaFoldDB; F1QWM2; -.
DR SMR; F1QWM2; -.
DR STRING; 7955.ENSDARP00000107352; -.
DR PaxDb; F1QWM2; -.
DR Ensembl; ENSDART00000167359; ENSDARP00000141748; ENSDARG00000099889.
DR GeneID; 792623; -.
DR CTD; 240892; -.
DR ZFIN; ZDB-GENE-140513-1; dusp27.
DR eggNOG; KOG1716; Eukaryota.
DR GeneTree; ENSGT00940000159723; -.
DR HOGENOM; CLU_009343_0_0_1; -.
DR OMA; FNTPCVM; -.
DR OrthoDB; 1576308at2759; -.
DR PRO; PR:F1QWM2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR Bgee; ENSDARG00000099889; Expressed in muscle tissue and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0033549; F:MAP kinase phosphatase activity; IBA:GO_Central.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0014866; P:skeletal myofibril assembly; IMP:ZFIN.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR020405; Atypical_DUSP_subfamA.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR45682; PTHR45682; 1.
DR Pfam; PF00782; DSPc; 1.
DR PRINTS; PR01909; ADSPHPHTASEA.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..1100
FT /note="Serine/threonine/tyrosine-interacting-like protein
FT 2"
FT /id="PRO_0000442054"
FT DOMAIN 141..289
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1031
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1100 AA; 122644 MW; 847CC9D416BE5A98 CRC64;
MASSVEDQQL QQEEAESVKD VQSHYLRCPS PSFSMMSDRF STVSDRFSVI SGSEAESIFM
EPIHLSSTIA AKKIISEELP PRPARVSSPP DSALEPAQQL MVEDLYSRVQ ELLDERSLYN
TPCVLDIQRA LLRDRLEAPL SPVDEVWPNV FIAEKSVAVN KGRLKRLGIT HVLNAAHGTG
VYTGPLFYSG MNIHYMGIEV DDFPDADISP HFRSCAEFLD DALLTHRGKV LVDSMMGVSR
SAVLVAAYLM IFQNMSIMEA LLEIRKKRAI SPNEGFIKQL RQLNETLMEE RDEDDDETLS
QCSVIDARGR LEEQESVFGV KADSIMVEEE EDGGGSVISS VASSAAAAAL RAGVQCGSQQ
PNMQQPADQP SLPGQTREDE DGDVDRMILE WQKRNEKYQS EDWWEAQLLC EDEDDGEDKT
QRAVRPDDLE SVTSEDVRMV KERIGRRPRR AASLAGSTSS CSSYVDLWKQ RLQELEEQAA
ARHRLQDQDT SSETQQKKID DDVQSILSDS SSMYNFCKKN KENLTPLERW KIKRIQFGWN
KKENAENGEQ SEAEPAAAPD LEDVNLTAYQ TWKLKQQKKH GGEENKEEIL QMSRGEDTAT
ARRRQRREEV LERSRRNLQE SQSVCGWETE SALSSSIPLS AFCAGAFPSA SVCGDDSMSV
LSGRSSVLSG RSTRSLPPAV LETPAPPTPV LGPNGEQMVN IANIQNWIAS VVNETLQQKQ
TEMLMGASVA PSRAGSVFSA GRGVDDDKSS VLSGLSASTG LSRSRAESVV SVGAKARSVL
SAAGRAESVF SAGGASQLSC GSRKSKITTT SVPLYSLFQD QVNLHKLDTM EKEIKSDMRD
KMASYEIKKI TEDNKRSTLY KKKKPKEDDE DVDIAKSNGL EELEARTCEK PKPKRDYGRS
GILNLPASAN NPTSSIDEWL EHVRPPSSKP RVYDGDSGPI RMSRPAYEEL QEPSGLDFTS
RRSSVSVEVD EEEDYSFRFS SRNCADDDLD PELSYSSRRS PSFNGLSEST SFASRRSYSR
YEDEERSSFQ NHSIKQKSSV YEDSGRTAGS RRDEEEDEEI SAFIAQIKQR ARARVAEEME
DDEVLTAWRK QEESKSHDHK
